Evidence map›Paper›PMID 33138280›Full record

ArticleInternational journal of molecular sciences2020

Vitamin B3-Based Biologically Active Compounds as Inhibitors of Human Cholinesterases.

Antonio Zandona, Gabriela Lihtar, Nikola Maraković, Katarina Miš, Valentina Bušić, Dajana Gašo-Sokač, Sergej Pirkmajer, Maja Katalinić

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.2field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 9 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Antonio ZandonaInstitute for Medical Research and Occupational Health, Ksaverska c. 2, HR-10001 Zagreb, Croatia.ORCID 0000-0002-3937-3520
Gabriela LihtarInstitute for Medical Research and Occupational Health, Ksaverska c. 2, HR-10001 Zagreb, Croatia.
Nikola MarakovićInstitute for Medical Research and Occupational Health, Ksaverska c. 2, HR-10001 Zagreb, Croatia.
Katarina MišInstitute of Pathophysiology, Faculty of Medicine, University of Ljubljana, Zaloska 4, SLO-1001 Ljubljana, Slovenia.
Valentina BušićFaculty of Food Technology Osijek, Josip Juraj Strossmayer University of Osijek, Kuhačeva 20, HR-31000 Osijek, Croatia.
Dajana Gašo-SokačFaculty of Food Technology Osijek, Josip Juraj Strossmayer University of Osijek, Kuhačeva 20, HR-31000 Osijek, Croatia.
Sergej PirkmajerInstitute of Pathophysiology, Faculty of Medicine, University of Ljubljana, Zaloska 4, SLO-1001 Ljubljana, Slovenia.
Maja KatalinićInstitute for Medical Research and Occupational Health, Ksaverska c. 2, HR-10001 Zagreb, Croatia.
Institute for Medical Research and Occupational Health · HRUniversity of Ljubljana · SIUniversity of Osijek · HR

Funding

GERIATRIC ASSESSMENT--MULTICENTER CONTROLLED EVALUATIONR01AG008276 · NIA · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SILVERMAN, MYRNA A · 1990 to 1993
–
Croatian Science Foundation HrZZ-IP-2018-01-7683Croatian Science Foundation HrZZ-UIP-2017-05-7260Ministry of Science and Education, Croatia Croatian-Slovenian Bilateral grant 2020-2021Slovenian Research Agency J7-8276Slovenian Research Agency P3-0043
6 · The paper itself

Abstract

We evaluated the potential of nine vitamin B3 scaffold-based derivatives as acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitors, as a starting point for the development of novel drugs for treating disorders with cholinergic neurotransmission-linked pathology. As the results indicate, all compounds reversibly inhibited both enzymes in the micromolar range pointing to the preference of AChE over BChE for binding the tested derivatives. Molecular docking studies revealed the importance of interactions with AChE active site residues Tyr337 and Tyr124, which dictated most of the observed differences. The most potent inhibitor of both enzymes with

Indexed as

Cell ProliferationAcetylcholinesteraseButyrylcholinesteraseCatalytic DomainCholinesterase InhibitorsGPI-Linked ProteinsHumansMolecular Docking SimulationNeuroblastomaNiacinamideStructure-Activity RelationshipTumor Cells, CulturedAcetylcholinesteraseACHE protein, humanBCHE protein, humanButyrylcholinesteraseCholinesterase InhibitorsGPI-Linked ProteinsNiacinamideAChEAlzheimer’sBChEcytotoxicityneurodegenerativenicotinamide

Identifiers

PMID33138280
PMCPMC7663184
OpenAlexW3095243327

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.